Antifreeze protein (AFP) is known to bind to a single ice crystal composed of hexagonally arranged waters, hexagonal ice. To investigate the effect of the AFP binding to a general ice block that is an assembly of numerous hexagonal ice crystals, thermodynamic properties, dynamics, and the crystal structure of the ice block were examined in the presence of type I AFP (AFP-I). Previously, it was found that hexagonal ice has a glass transition based on the proton ordering in the ice lattice at low temperature. Measurements of heat capacity under adiabatic conditions, dielectric permittivity, and powder X-ray diffraction revealed that the glass transition occurs around 140 K in the ice containing 0.01-1% (w/w) of the AFP-I, which is greater than the value for the pure hexagonal ice (ca. 110 K). These data imply that AFP affects the glass transition kinetics, i.e., the slowness of the proton migration in the ice block. Hence, adsorption of AFP molecules to each hexagonal ice is thought to change the physicochemical properties of the bulk ice.